The invention relates to a process for the preparation of a melanic pigment, comprising the polymerisation of a compound corresponding to the formula: ##STR1## in which: R denotes a hydrogen atom, an alkyl, alkoxy, hydroxyalkyl, SiR4 R5 R6 or aminoalkyl radical, or an aryl radical which is unsubstituted or substituted by OH, NH2, alkyl, alkoxy or NO2 ;
R1 and R2 denote alkyl groups or together form a methylene or ethylene group which is optionally substituted by one or more alkyl groups, and R2 denotes hydrogen or COOH, in the presence of an oxidizing medium and of an enzyme with (per)oxidizing activity or of a compound which has a similar activity, and to powders which make use of them and to their cosmetic use.
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1. A process for the preparation of a melanic pigment comprising polymerizing in a polymerization medium a compound having the formula ##STR3## wherein R represents hydrogen, alkyl, alkoxy, hydroxyalkyl, aminoalkyl or SiR4 R5 R6 wherein R4, R5 and R6 represent alkyl containing 1-8 carbon atoms or aryl unsubstituted or substituted by OH, NH2, alkyl, alkoxy or NO2,
R1 and R2, each independently, represent lower alkyl, or R1 and R2 taken together form a methylene or ethylene group optionally substituted by one or more lower alkyl groups, and R3 represents hydrogen or COOH, said polymerization medium comprising (i) hydrogen peroxide or oxone as an oxidizing medium and (ii) horseradish peroxidase as an enzyme having (per) oxidizing activity or haemoglobin as a compound having a (per) oxidizing activity.
2. A process for the preparation of a melanic pigment comprising polymerizing in a polymerization medium a compound having the formula ##STR4## wherein R represents hydrogen, alkyl, alkoxy, hydroxyalkyl, aminoalkyl or SiR4 R5 R6 wherein R4, R5 and R6 represent alkyl containing 1-8 carbon atoms or aryl unsubstituted or substituted by OH, NH2, alkyl, alkoxy or NO2,
R1 and R2, each independently, represent lower alkyl, or R1 and R2 taken together form a methylene or ethylene group optionally substituted by one or more lower alkyl groups, and R3 represents hydrogen or COOH, said polymerization medium comprising (i) an oxidizing medium and (ii) at least one of (1) an enzyme having (per)oxidizing activity and selected from the group consisting of horseradish peroxidase, chloroperoxidase, milk peroxidase, cytochrome C peroxidase and microperoxidase, (2) a compound having (per)oxidizing activity and selected from the group consisting of haemoglobin, myoglobin, methaemoglobin and metmyoglobin and (3) an enzyme having oxidizing activity and selected from the group consisting of an alcohol-oxidase, a polyphenol-oxidase and a dealkylating monooxygenase. 3. The process of
4. The process of
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The invention relates to a new process for the preparation of melanic pigments by an enzyme route, and to their use, especially in cosmetics.
The use of colored pigments is of very great interest in the cosmetic field.
It involves essentially inorganic pigments or pigments originating from synthetic direct colorants, or from pure carbon in the case of black pigments.
These various products can present problems in use, and some of them are not completely harmless.
It is known that yellow-brown colorants can be produced by oxidizing 5-hydroxyindole with horseradish peroxidase in the presence of aqueous hydrogen peroxide. This colorant consists of 5-hydroxyindole dimers and trimers (A. Napolitano et al., Tetrahedron, Vol. 44, No. 23, pages 7265-7270--1988).
It is also known that 9-methoxyellipticine can be demethylated with horseradish peroxidase in the presence of aqueous hydrogen peroxide to form chiefly 9-oxo-ellipticine (Gerard Meunier et al., J. Am. Chem. Soc., 1985, 107, 2558-2560). This process enables the quinone imine to be obtained in yields of at least 90%.
The Applicants have surprisingly found that melanic pigments can be prepared by an enzyme route, by oxidative polymerization of 5,6-dihydroxyindole derivatives in which the hydroxyl functional groups are blocked. These 5,6-dihydroxyindole derivatives have the advantage of being stable and relatively low in cost.
The pigment obtained by this process is easier to incorporate into cosmetic compositions because of its ease of dispersion and its small particle size.
The subject of the invention consists, therefore, of a process for the preparation of a melanic pigment and the pigment thus obtained.
The name "melanic pigment" is given to the pigment resulting from the oxidative polymerization of precursors related to indole; this pigment is identical with, or similar to, melanin.
Other subjects of the invention will become apparent on reading the description and the examples which follow.
The process for the preparation of the melanic pigment is essentially characterised in that a compound is polymerized which corresponds to the formula: ##STR2## in which: R denotes a hydrogen atom or an alkyl, alkoxy, hydroxyalkyl, aminoalkyl or SiR4 R5 R6 radical, where R4, R5 and R6 denote an alkyl group, in which the alkyl residue contains from 1 to 8 carbon atoms, or an aryl radical which is unsubstituted or substituted by OH, NH2, alkyl, alkoxy or NO2 ;
R1 and R2, which are identical or different, denote alkyl groups or together form a methylene or ethylene group which is optionally substituted by one or more alkyl groups, and R2 denotes a hydrogen atom or the COOH radical, in the presence of an oxidizing medium and of an enzyme with (per)oxidizing activity or of a compound which has a similar activity.
The alkyl or alkoxy radicals preferably denote lower radicals containing 1 to 6 carbon atoms; aryl preferably denotes phenyl.
The compounds corresponding to the formula (I) shown above are preferably chosen from 5,6-dimethoxyindole, 5,6-methylenedioxyindole and 1-methyl 5,6-dimethoxyindole.
The oxidizing medium may consist of peroxides such as hydrogen peroxide or persalts such as potassium monopersulphate (oxone), or of atmospheric oxygen, depending on the nature of the enzymes with oxidizing activity which are used.
These enzymes, with peroxidizing activity, are chosen from horseradish peroxidase, chloroperoxidase, milk peroxidase, cytochrome C peroxidase and microperoxidase.
The compounds which have an activity similar to that of the enzymes with peroxidizing activity are chosen from crude or purified haemoglobin, myoglobin, methaemoglobin and metmyoglobin.
The enzymes with oxidizing activity are chosen from alcohol-oxidases such as methanol-oxidase, polyphenol-oxidases, or dealkylating monooxygenases such as the enzymes produced by the microorganism Pseudomonas testosteroni. D. W. Ribbons, FEBS Letters, 8 (1970), p.101).
Horseradish peroxidase, haemoglobin and methaemoglobin are particularly preferred.
In the case of haemoglobin, potassium ferricyanide may be added to the reaction mixture to convert it into methaemoglobin.
When haemoglobin, myoglobin, methaemoglobin or metmyoglobin is employed, an inorganic salt like ammonium sulphate or an organic product such as formamide or guanidine in the form of hydrochloride may be added to the reaction mixture.
The concentration of hydrogen peroxide employed with the enzymes with peroxidizing activity is low and generally lower than 5% by weight relative to the total weight of the reaction mixture and preferably lower than 2%, the minimum concentration being 0.007%.
The concentration of persalt is between 2 and 600 millimoles/liter.
In the case of methanol-oxidase, this is employed in the presence of methanol or ethanol and atmospheric oxygen as oxidising agent.
The weight relationship between the indole-related derivative of formula (I) and the enzyme with oxidizing activity or the compound which has a similar activity may vary in wide proportions ranging from 1 to 106.
The preparation of the melanic pigment is generally performed at a pH which is compatible with the enzymes used and is generally between 2 and 11, and preferably between 4 and 8. This pH is obtained with the aid of a buffer which is appropriate to the enzyme in question, such as, for example, an acetate buffer, a phosphate buffer or a citrate buffer.
The reaction temperature is compatible with the enzymes employed and is generally between 10°C and 50°C and preferably between 20° and 45°C
The reaction medium generally consists of water or a mixture of water and organic solvent. In some cases this medium may consist solely of an organic solvent when hydroperoxides other than hydrogen peroxide are employed.
The solvents which may be employed are chosen especially from aromatic hydrocarbons such as toluene, or esters such as ethyl acetate, or dimethylformamide, N-methylpyrrolidone, dimethyl sulphoxide, dioxane and acetone.
The formation of the melanic pigment must be performed in conditions which are such as to have a good dispersion of the enzyme in the reaction mixture. It may thus be performed by immobilizing the enzyme on the surface of a suitable support, or else a chemically modified enzyme may be employed so as to facilitate its solubilization in the reaction mixture.
A preferred embodiment consists in immobilizing horseradish peroxidase by the technique of drying the enzyme with air on the surface of glass beads, as described in the Journal of American Chemical Society, 107, 5448, by R. Z. Kazantjian and Klibanov, 1985.
In a preferred embodiment an enzyme with peroxidizing activity is added to a solution of indole-related precursor of formula (I) in an aqueous solvent medium and, after 1 to 30 minutes, a solution of hydrogen peroxide is added. After 1 to 24 hours a brown-to-black precipitate is separated off by filtration, centrifuging or freeze-drying. This precipitate is optionally washed with water or with an organic solvent such as those mentioned above and is then dried.
The pigments according to the invention may be characterized by EPR (electron paramagnetic resonance) with the aid of a Brucker ER 200 D spectrometer at 9.52 GHz with a field modulation frequency of 100 kHz and a microwave power of 1.9 mW. The absorption of this wave by the pigment as a function of the field is recorded and a maximum absorption is found at about 3480 gauss. This absorption maximum is also found in natural eumelanins.
The melanic pigment thus prepared can be employed in diverse applications where it is desired to have available a brown-to-black pigment, such as especially in cosmetics in make-up products, sun compositions and hair-coloring products.
With a view to these applications they may be introduced into a cosmetically acceptable medium based on water or on mixtures of water and organic solvent(s) or on one or more solvents, and optionally other additives usually employed in cosmetics, such as surface-active agents, thickeners, stabilizers, etc.
According to an alternative form of the invention, the melanic pigment may be deposited onto an inorganic filler consisting of inert particles which have a particle size smaller than 20 microns and preferably 10 microns. The pigment may also be deposited and/or absorbed onto an organic filler consisting of polymer particles which have a particle size smaller than 100 microns or onto a crosslinked polymeric material forming microspheres, as described in application EP 313,380.
According to another alternative form the pigment may be deposited and/or absorbed onto organic or inorganic particles with a lamellar structure smaller than 50 microns by the largest dimension.
A powder whose color shades range from brown to black is thus obtained, and can be employed in cosmetics.
According to this alternative form this colored powder may be prepared by dispersing the inorganic or organic particles in the solution of indole-related precursor of formula (I) containing the enzyme. The conditions of oxidation of the precursor of formula (I) are identical with those described above and, especially in the case where an enzyme or a compound with activity similar to peroxidizing activity is employed, the solution additionally contains hydrogen peroxide or a persalt.
After 1 minute to 24 hours of reaction, the powder containing the pigment is separated off by filtration, is washed with water or with an organic solvent and is dried.
This powder can also be prepared by absorbing the melanic pigment prepared in accordance with the invention onto and into the inorganic or organic particles defined above.
The procedure, in particular, is to disperse the melanic pigment formed beforehand in a medium which is a nonsolvent for the particles and contains the said particles, and after pigment absorption these are dried.
More particularly, particles of calcium carbonate or of silica which have a particle size generally greater than 0.01 micron are employed as the inorganic filler.
The organic filler employed is preferably particles of polymers derived from optionally modified keratin, of polymers derived from optionally deacetylated chitin, of silk fibroin, of synthetic polymers chosen from crosslinked polymethyl methacrylate, crosslinked poly-β-alanine, hollow microspheres of vinylidene chloride/acrylonitrile copolymer or porous microspheres of polyamide 12, polyamide 6 or copolyamide 6/12, of silicone powders consisting of gums, resins or organopolysiloxane elastomers.
These particles have a particle size which is preferably greater than 0.01 micron.
As the crosslinked polymeric material there may be mentioned microspheres of styrene/divinylbenzene or methyl methacrylate/ethylene glycol dimethacrylate, whose particle size is preferably between 5 and 100 microns.
The organic or inorganic particles with lamellar structure which are employed are preferably L-lauroyllysine, ceramic microparticles optionally coated with zirconium powder, lamellar titanium dioxide, lamellar talc, boron nitrite, mica and bismuth oxychloride. These particles have a particle size which is preferably larger than 0.5 micron and smaller than 50 microns, the relationship between the largest dimension and the thickness being between 2 and 100.
The examples which follow are intended to illustrate the invention without, however, being limiting in nature.
PAC Preparation of a melanic pigment from 5,6-dimethoxyindole0.378 g of horseradish peroxidase (Sigma) and 1 g of 5,6-dimethoxyindole in 8 ml of DMF are added to 4 liters of a sodium acetate buffer (20 nMoles-pH 5).
15 minutes after the addition of the enzyme, 8 ml of 110-volume aqueous hydrogen peroxide are added.
The reaction mixture is left stirred for 6 hours and then left to stand overnight at room temperature. After centrifuging followed by washing with water, the black pigment is dried under vacuum.
EPR analysis shows a maximum absorption at about 3480 gauss.
PAC Preparation of a melanic pigment from 5,6-methylenedioxyindole.0.6 g of horseradish peroxidase (Sigma) and 1.6 g of 5,6-methylenedioxyindole in 13 ml of dimethylformamide are added to 6.4 l of a sodium acetate buffer (20 nMoles-pH 5).
15 minutes after the addition of the enzyme, 12.8 ml of 110-volume aqueous hydrogen peroxide are added.
The reaction mixture is left at room temperature for 36 hours. After centrifuging followed by washing with water, the black pigment obtained is dried under vacuum.
EPR analysis shows a maximum absorption at about 3480 gauss.
PAC Preparation of a melanic pigment from 5,6-dimethoxyindole.After dissolving at room temperature, with stirring, 1 g of commercial haemoglobin sold by Sigma in 50 cm3 of 0.1M sodium citrate-citric acid buffer solution, adjusted to pH=5.5, 30 g of ammonium sulphate are added. After stirring for 1/2 an hour, the solution is centrifuged for 20 minutes at 10,000 revolutions/minute. The haemoglobin deposited is taken up with 500 cm3 of 0.1M sodium acetate-acetic acid buffer solution, adjusted to pH=5 and brought to a temperature of 37°C 60 mg of potassium ferricyanide are added to the solution, followed 1/2 an hour later by 1 g of 5,6-dimethoxyindole dissolved in 4 cm3 of dimethylformamide. 4 cm3 of l10-volume aqueous hydrogen peroxide are then poured in with vigorous stirring.
The reaction mixture is left stirred at 37°C for 4 hours and is then centrifuged. The pigment is greenish in color. The black pigment is obtained by washing with dimethylformamide, with acetone and then with water, and is dried under vacuum.
EPR analysis shows a maximum absorption at about 3480 gauss.
PAC Preparation of a melanic pigment from 5,6-dimethoxyindole.1 g of commercial haemoglobin sold by Sigma is dissolved with stirring in 100 cm3 of distilled water at room temperature. After dissolving, 1 g of 5,6-dimethoxyindole in 4 cm3 of dimethylformamide is poured in, followed by 3.4 g of oxone (potassium monopersulphate triple salt) powder. The reaction mixture is left for 5 minutes at room temperature with stirring and is then centrifuged. The pigment is greenish in color. The black pigment is obtained by washing with dimethylformamide, with acetone and then with water, and is dried under vacuum.
EPR analysis shows a maximum absorption at about
PAC Preparation of a melanic pigment from 5,6-dimethoxyindole.1 g of commercial haemoglobin sold by Sigma is dissolved in 500 cm3 of sodium acetate-acetic acid buffer, adjusted to pH=5 and containing 0.1 g of formamide (or 0.1 g of guanidinium hydrochloride). After stirring for 1 hour at 37°C, 1 g of 5,6-dimethoxyindole in 4 cm3 of DMF is added, followed by 4 cm3 of 110-volume aqueous hydrogen peroxide. The reaction mixture is left stirred at 37° for 4 hours and is then centrifuged. The black pigment obtained is washed with DMF, with acetone and then with water and is dried under vacuum.
EPR analysis shows a maximum absorption at about 3480 gauss.
PAC Preparation of a melanic pigment from 5,6-dimethoxyindole.1 g of commercial haemoglobin sold by Sigma is dissolved in 500 cm3 of sodium acetate-acetic acid buffer, adjusted to pH=5.1 g of 5,6-dimethoxyindole in 4 cm3 of DMF is added, followed by 4 cm3 of 110-volume aqueous hydrogen peroxide. The reaction mixture is left stirred at 37°C for 4 hours and is then centrifuged. The brown pigment obtained is washed with DMF, with acetone and then with water, and is dried under vacuum.
EPR analysis shows a maximum absorption at about 3480 gauss.
PAC Preparation of a melanic pigment from 1-methyl-5,6-dimethoxyindole.After dissolving at room temperature, with stirring, 1 g of commercial haemoglobin sold by Sigma in 50 cm3 of 0.1M sodium citrate-citric acid buffer solution, adjusted to pH=5.5, 30 g of ammonium sulphate are added. After stirring for 1/2 an hour, the solution is centrifuged for 20 minutes at 10,000 revolutions/minute. The haemoglobin deposited is taken up with 500 cm3 of 0.1M sodium acetate-acetic acid buffer solution, adjusted to pH=5 and brought to a temperature of 37°C 60 mg of potassium ferricyanide are added to the solution. The mixture is left for 1/2 an hour with vigorous stirring and then 1 g of 1-methyl-5,6-dimethoxyindole dissolved in 4 cm3 of DMF is added to it, followed by 4 cm3 of 110-volume aqueous hydrogen peroxide.
The reaction mixture is left stirred at 37°C for 4 hours and is then centrifuged. The brown pigment obtained is washed with DMF, with acetone and then with water, and is dried under vacuum.
EPR analysis shows a maximum absorption at about 3480 gauss.
| ______________________________________ |
| EXAMPLE A: MASCARA CREAM |
| Black pigment obtained according |
| 15.0 g |
| to Example 1 |
| Triethanolamine stearate 15.0 g |
| Candelilla wax 8.0 g |
| Carnauba wax 10.0 g |
| Hydroxyethyl cellulose 0.9 g |
| Keratin hydrolyzate (expressed as dry |
| 0.75 g |
| substance) |
| Stabilizers q.s. |
| Water q.s. 100.0 g |
| The pigment obtained in Example 3 may be employed instead |
| of that obtained in Example 1. |
| EXAMPLE B: HAIR GEL |
| Black pigment obtained according |
| 0.5 g |
| to Example 2 |
| Vinylpyrrolidone/vinyl acetate copolymer |
| 1.5 g |
| sold under the name PVP/VA S 630 |
| by GAP |
| Ethyl alcohol 15.0 g |
| Carbopol 940 (Goodrich Chemical) |
| 0.7 g |
| Triethanolamine q.s. pH = 7.5 |
| Stabilizers q.s. |
| Water q.s. 100.0 g |
| The pigment obtained in Example 5 may be employed instead |
| of that obtained in Example 2. |
| ______________________________________ |
Junino, Alex, Andrean, Herve, Tuloup, Remi, Higgins, Irwing J.
| Patent | Priority | Assignee | Title |
| 5538517, | Jun 25 1992 | L'Oreal | Method for dyeing keratin fibers with indole or indoline derivatives, hydrogen peroxide and a peroxidase |
| 5645609, | Aug 01 1991 | L'Oreal | Compositions which contain and processes which use an insoluble pigment obtained by the oxidative polymerization of indole derivatives for the temporary dyeing of keratinous fibers |
| 5750093, | Apr 30 1993 | DUSA PHARMACEUTICALS, INC. | 33 Lipomelanin sunscreen composition |
| 5776241, | Apr 27 1993 | L'Oreal | Process for the preparation of a melanic pigment of small particle size and its use in cosmetics |
| 5776497, | Jan 16 1992 | L'Oreal | Product based on inorganic or organic particles bearing an indoline-based product |
| 5827330, | Dec 06 1995 | Clairol Incorporated | Synthesis of quarternary melanin compounds and their use as hair dyes or for skin treatment |
| 5874091, | Sep 27 1990 | L'Oreal | Cosmetic composition comprising a dispersion of lipid vesicles as well as melanin pigments |
| 5954871, | Dec 16 1996 | L Oreal | Composite melanin pigment in the form of particles comprising a wax-based spherical core, preparation processes and cosmetic uses |
| 6274131, | Dec 31 1997 | L OREAL S R | Mascara comprising a mixture of hard waxes and of film-forming polymer |
| 6303106, | Dec 07 1995 | CRODA INTERNATIONAL PLC | Allomelanin production |
| 6316012, | Sep 01 1992 | L'Oreal | Cosmetic or pharmaceutical composition comprising, in combination, a peroxidase and an anti-singlet oxygen agent |
| Patent | Priority | Assignee | Title |
| 4776857, | Nov 21 1986 | Repligen Corporation | Use of hydroxylated indoles as dye precursors |
| 4804385, | Jan 20 1986 | L'Oreal | Process for dyeing keratinous fibres with 5,6-dihydroxy-indole combined with an iodide and dyeing composition employed |
| 4822375, | Mar 06 1986 | L OREAL | Dyeing compositions for keratinous fibres based on indole derivatives, and new compounds |
| 4888027, | Apr 02 1987 | L'Oreal | Process for dyeing keratinous fibers with 5,6-dihydroxyindole in combination with an iodide and a hydrogen peroxide composition at alkaline pH |
| 4961754, | Jul 17 1987 | L'Oreal | Ultrafine inorganic powder containing melanin pigments, process for preparation thereof and its use in cosmetics |
| 5011500, | Dec 30 1987 | L'Oreal | Process for dyeing keratinous fibres and dye composition employing indole derivatives and direct nitro dyes |
| 5021067, | Feb 08 1988 | L'Oreal | Composition for dyeing keratinous fibres employing an indole dye and at least one para-phenylenediamine disubstituted on one of the amino groups and process employing it |
| 5034015, | Sep 12 1988 | L'Oreal | Process for dyeing keratin fibres with a monohydroxyindole associated with an iodide and hydrogen peroxide |
| 5073174, | Jul 21 1989 | L'Oreal | Dyeing process employing indole dyes and oxidation dye precursors and dyeing agents employed |
| GB2207153, |
| Executed on | Assignor | Assignee | Conveyance | Frame | Reel | Doc |
| Jan 31 1991 | JUNINO, ALEX | L Oreal | ASSIGNMENT OF ASSIGNORS INTEREST | 005640 | /0387 | |
| Jan 31 1991 | ANDREAN, HERVE | L Oreal | ASSIGNMENT OF ASSIGNORS INTEREST | 005640 | /0387 | |
| Jan 31 1991 | TULOUP, REMI | L Oreal | ASSIGNMENT OF ASSIGNORS INTEREST | 005640 | /0387 | |
| Jan 31 1991 | IRWING, JOHN HIGGINS | L Oreal | ASSIGNMENT OF ASSIGNORS INTEREST | 005640 | /0387 | |
| Feb 05 1991 | L'Oreal | (assignment on the face of the patent) | / | |||
| Feb 08 1991 | KENT-MOORE CORPORATION, A CORP OF DE | GRACO INC , A CORP OF MN | ASSIGNMENT OF ASSIGNORS INTEREST | 005640 | /0216 |
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